2qp9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:2qp9.jpg|left|200px]]
{{Seed}}
[[Image:2qp9.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qp9|  PDB=2qp9  |  SCENE=  }}  
{{STRUCTURE_2qp9|  PDB=2qp9  |  SCENE=  }}  


'''Crystal Structure of S.cerevisiae Vps4'''
===Crystal Structure of S.cerevisiae Vps4===




==Overview==
<!--
The multivesicular body (MVB) pathway functions in multiple cellular processes including cell surface receptor down-regulation and viral budding from host cells. An important step in the MVB pathway is the correct sorting of cargo molecules, which requires the assembly and disassembly of endosomal sorting complexes required for transport (ESCRTs) on the endosomal membrane. Disassembly of the ESCRTs is catalyzed by ATPase associated with various cellular activities (AAA) protein Vps4. Vps4 contains a single AAA domain and undergoes ATP-dependent quaternary structural change to disassemble the ESCRTs. Structural and biochemical analyses of the Vps4 ATPase reaction cycle are reported here. Crystal structures of Saccharomyces cerevisiae Vps4 in both the nucleotide-free form and the ADP-bound form provide the first structural view illustrating how nucleotide binding might induce conformational changes within Vps4 that lead to oligomerization and binding to its substrate ESCRT-III subunits. In contrast to previous models, characterization of the Vps4 structure now supports a model where the ground state of Vps4 in the ATPase reaction cycle is predominantly a monomer and the activated state is a dodecamer. Comparison with a previously reported human VPS4B structure suggests that Vps4 functions in the MVB pathway via a highly conserved mechanism supported by similar protein-protein interactions during its ATPase reaction cycle.
The line below this paragraph, {{ABSTRACT_PUBMED_17949747}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17949747 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17949747}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Transport]]
[[Category: Transport]]
[[Category: Vacuole]]
[[Category: Vacuole]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:21:24 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:54:27 2008''

Revision as of 17:54, 27 July 2008

File:2qp9.png

Template:STRUCTURE 2qp9

Crystal Structure of S.cerevisiae Vps4

Template:ABSTRACT PUBMED 17949747

About this Structure

2QP9 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4., Xiao J, Xia H, Yoshino-Koh K, Zhou J, Xu Z, J Mol Biol. 2007 Nov 30;374(3):655-70. Epub 2007 Sep 29. PMID:17949747

Page seeded by OCA on Sun Jul 27 20:54:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2qp9&oldid=666606"